水晶體 β-Crystallin의 Carboxylmethylation에 關한 硏究 = Studies on Carboxylmethylation of β-Crystallin of Bovine Lens

다국어 초록 (Multilingual Abstract)

Changes of protein patterns of nonmethylated and endogenous or exogenous methylated β-crystallin fractions have been investigated, and then the methyl-acceptor proteins identified by urea /polyacrylamide gel electrophoresis.
1. Nonmethylated β_H and β_L-crystallin were separated in ten, eleven fractions, respectively. In the endogenous methylated β_H-crystallin, subfraction No. 10 was disappeared and No.3 was increased when compared with that of nonmethylated. In the β_L-cryallin, subfraction No.8, 10, 11 were decreased and No.6, 7 was increased.
2. When native β-crystallins were electrophoresed, subfraction No. 7, 9 disappeared and No.8b, 10b were newly appeared and. No. 6 was increased in methylated β_H-crystallin, and subfraction No. 11 was disappeared, No.9 was decreased and No.8 was increased in meth ylated β_L-crystallin. But, subfraction profile of methylted a-crystallin was not changed.
3. Methyl-acceptor proteins in each crystallin were subfraction No. 1, 6, 8 in a-crystallin, 2, 3, 6, l0a in β_H-crystallin and 1, 6, 7, 8, 10 in β_L-crystallin, respectively.
These results suggest that the effect of carboxylmethylation on the aggregation of β-crystallin is related to not only the interaction of a, r-crystallin subfractions, but also the interaction of β-crystallin subfractions. On the other hand, a-crystallin is only related to the interaction of the other crystallin subfractions.